Meeting Abstract
P1.93 Jan. 4 Comparison of Stess Protein cDNA and Amino Acid Sequences Among Three Bee Species in Different Thermal Environments HALON, L.*; HRANITZ, J.M.; BRUBAKER, K.D.; YOCUM, G.D.; BARTHELL, J.F.; Bloomsburg University of Pennsylvania; Bloomsburg University of Pennsylvania; Bloomsburg University of Pennsylvania; USDA Laboratory, Fargo ND; University of Central Oklahoma, Edmond lthalon@bloomu.edu
The 70 kDa and 90 kDa stress proteins, heat shock proteins 70 (HSP70) and 90 (HSP90) respectively, are among the most important stress proteins in the eukaryotic cytosol. While we better know the ecological significance of stress proteins, evolutionary mechansims that maintain structure and function among taxa in diverse habtiats is still developing. Because expression and function of stress proteins are essential to the normal development and survival of species under a wide range of environmental conditions, evolution of stress proteins should favor structural changes in genetic code, gene expression, post-translational modification to maintain protein structure and organismal function in the environment. To study stress protein structure evolution in different environments, we compared cDNA and translated protein sequences of homologous regions in the ATPase domain of HSP70 and HSP90 in a leafcutting bee (Megachile apicalis) whose larvae tolerate heat stress to 50 C. We compared M. apicalis HSP70 and HSP90 sequences to homologous sequences in M. rotundata and Apis mellifera, two species of lower thermotolerance. Alignments showed that HSP70 cDNA and amino acid sequences were most similar between the more distantly related A. mellifera and M. rotundata than the two species of leafcutting bees. In contrast, alignments showed that HSP90 cDNA and amino acid sequences were most similar between the two closely related leafcutting bee species than between either leafcutting bee species and A. mellifera. Thus, amino acid substitutions in the homologous ATPase region of HSP70 of M. apicalis probably relate to HSP70 function in natural environments.
